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2 edition of Crystal structure studies of human erythrocyte carbonic anhydrase C at high resolution. found in the catalog.

Crystal structure studies of human erythrocyte carbonic anhydrase C at high resolution.

Anders Liljas

Crystal structure studies of human erythrocyte carbonic anhydrase C at high resolution.

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Published by Universitet, Almqvist & Wiksell (distr.) in Uppsala, Stockholm .
Written in English

    Subjects:
  • Carbonic anhydrase.,
  • X-ray crystallography.

  • Edition Notes

    SeriesActa Universitatis Upsaliensis., 3
    Classifications
    LC ClassificationsQD945 .L45
    The Physical Object
    Paginationix, 106 p.
    Number of Pages106
    ID Numbers
    Open LibraryOL5325725M
    LC Control Number72178549

    Carbonic anhydrase 4 is an enzyme that in humans is encoded by the CA4 gene. Function. Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and Aliases: CA4, CAIV, Car4, RP17, carbonic anhydrase 4.


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Crystal structure studies of human erythrocyte carbonic anhydrase C at high resolution. by Anders Liljas Download PDF EPUB FB2

Mol. Biol. () 12, Crystal Structure Studies on Human Erythrocyte Carbonic Anhydrase C. (II)t BJORN TILANDER, BROR STRANDBERG AND KERSTIN FRIDBORf~ Institutes of Chemistry and Biochemistry University of Uppsala, Uppsala, Swe&n (Received 19 Decemberand in revlsed form 26 March ) Several heavy-atom derivatives of human carbonic anhydrase form C have been Cited by: The three-dimensional structure of carbonic anhydrase B (EC 4,2,1,1; carbonate hydro-lyase) from human erythrocytes has been determined to high resolution.

Parallel and antiparallel pleated sheet makes up the predominant secondary structure of the by: Crystal structure studies of human erythrocyte carbonic anhydrase C at high resolution Liljas, Anders Uppsala University, Disciplinary Domain of Science and Technology. The first X-ray crystal structures of CA reported in s were the structures α-CA isoforms of CA I and CA II purified from human erythrocytes [18] [19] [20][21].

CA I crystals usually form the. Tilander B, Strandberg B, Fridborg K () Crystal structure studies on human erythrocyte carbonic anhydrase C. J Mol Biol – Google Scholar Tu C, Silvermann DN () Comparison of exchange catalyzed by isoenzymes of carbonic by: Structural Relationship of Human Erythrocyte Carbonic Anhydrase Isozymes B and C Notstrand, B., Vaara, I., Kannan, K.K.

() Isozymes-molecular Structure 1: ; Crystal Structure of Human Erythrocyte Carbonic Anhydrase C. The Three-Dimensional Structure at High Resolution in Relation to Other Mammalian Carbonic AnhydrasesCited by:   Crystal structure of Crystal structure studies of human erythrocyte carbonic anhydrase C at high resolution.

book carbonic anhydrase II at Å resolution in complex with coumate, a novel anti-cancer agentCited by: Structural Relationship of Human Erythrocyte Carbonic Anhydrase Isozymes B and C Notstrand, B.,Vaara, I.,Kannan, K.K.

() Isozymes-Molecular Structure 1: ; Crystal Structure of Human Erythrocyte Carbonic Anhydrase C. The Three-Dimensional Structure at High Resolution in Relation to Other Mammalian Carbonic AnhydrasesCited by: The structure of human erythrocytic carbonic anhydrase II has been refined by constrained Crystal structure studies of human erythrocyte carbonic anhydrase C at high resolution.

book restrained structure-factor least-squares refinement at A resolution. The conventional crystallographic R value is %. Of solvent molecules associated with the protein, four are buried and stabilize secondary structure by: () Isozymes-Molecular Structure 1: ; Refined Structure of Human Carbonic Anhydrase II at Angstroms Resolution Eriksson, A.E.,Jones, T.A.,Liljas, A.

() Proteins 4: ; Crystal Structure of Human Erythrocyte Carbonic Anhydrase C. The Three-Dimensional Structure at High Resolution in Relation to Other Mammalian Carbonic AnhydrasesCited by: Click on the article title to read more. Kannan KK, Liljas A, Waara I, Bergsten P-C, Lovgren S, Strandberg B, Bengtsson U, Carlbom U, Fridborg K, Järup L, Petef M () Crystal structure of human erythrocyte carbonic anhydrase C.

The three-dimensional structure at high resolution in relation to other mammalian carbonic Cited by: 3. Fridborg, K. et al. Crystal structure of human erythrocyte carbonic anhydrase C Molecular structure of enzyme and of one enzyme-inhibitor complex at Å resolution Cited by: Crystal Structure of Human Erythrocyte Carbonic Anhydrase C.

Crystal structure studies of human erythrocyte carbonic anhydrase C at high resolution. book Three-dimensional Structure at High Resolution in Relation to Other Mammalian Carbonic Anhydrases. Cold Spring Harbor Symp.

on Quant. Biol., 36, Cited by: Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at Å resolution.

buttresse s the high-energ y Pro–Thr c onfor mation. Liljas, Crystal Structure Studies of Human Erythrocyte Carbonic Anhydrase C at High Resolution, Acta Universitatis Upsaliensis (Almqvist & Wiksell, Stockholm, ).

[4] J.E. Coleman, J. Biol. Chem. () [5]Cited by: The primary structure of human erythrocyte carbonic anhydrase C has been determined. The single polypeptide chain contains amino acid residues devoid of disulfide bridges. The experimental approach has involved restriction of the action of trypsin to.

More detailed discussions of specific aspects are discussed elsewhere in these proceedings (cf. this vol. Lindskog, D.N. Silverman, and others).

The present review is limited largely to data on the major human erythrocyte carbonic anhydrases whose crystal structure is now known to high by: 8.

The crystal structure of human carbonic anhydrase II (CA II) complexed with the inhibitor acetazolamide (AZM) has been determined at A resolution and refined to.

Recently, several studies have shown nitrite reductase activity of mammalian carbonic anhydrase II (CAII), yet the molecular basis for this activity is unknown. Here we report the crystal structure of copper-bound human CAII (Cu–CAII) in complex with NO 2 − at Å resolution.

The structure exhibits Type 1 (T-1) and 2 (T-2) copper centers. Carbonic anhydrases (CAs, EC ) catalyse the interconversion between CO2 and bicarbonate as well as other hydrolytic reactions. Among the six genetic families known to date, the α- β- γ- δ- ζ- and η-CAs, detailed kinetic and X-ray crystallographic studies have allowed a deep understanding of the structure–function relationship in this superfamily of proteins.

A metal Cited by: Crystal structure studies of human erythrocyte carbonic anhydradse at high resolution. Acta Universitatis Upsaliensis, Uppsala Dissertations Crystal structure of human erythrocyte carbonic anhydrase C. III. Molecular structure of the enzyme and of one enzyme inhibitor complex at Å resolution.

Mol. Biol., 25, Activated by histamine, imidazole, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. Inhibited by coumarins, sulfonamide derivatives such as acetazolamide, benzenesulfonamide and derivatives (4-carboxyethylbenzene-sulfonamide, 4-carboxyethylbenzene-sulfonamide ethyl ester, 4-(acetylaminoethyl)benzene-sulfonamide, 4-aminoethylbenzene-sulfonamide), and 'prong inhibitors' BR The first α CA crystal structure of CA II was determined to Å resolution by Liljas et al.

in and further refined by Eriksson et al. in to the space group P2 1 with cell dimensions a =b =c = Å, and β = °. The overall shape of the molecule is an ellipsoid with dimensions ~40x40x50 Å. The conically shaped active site is ~15 Å deep with the catalytic Cited by: Carbonic anhydrase (CA; carbonate hydro-lyase, EC ) is a zinc-containing enzyme that catalyzes the reversible hydration of carbon dioxide: CO 2 + H 2 O ↔ HCO 3 − + H +.The enzyme is the target for drugs, such as acetazolamide, methazolamide, and dichlorphenamide, for the treatment of by: X-ray absorption studies of halide binding to carbonic anhydrase.

Bengtsson U, Carlbom U, Fridborg K, Järup L, et al. Crystal structure of human erythrocyte carbonic anhydrase C. The three-dimensional structure at high resolution in relation to other mammalian carbonic by: 9. @article{osti_, title = {A High-Resolution Crystal Structure of a Psychrohalophilic α–Carbonic Anhydrase from Photobacterium profundum Reveals a Unique Dimer Interface}, author = {Somalinga, Vijayakumar and Buhrman, Greg and Arun, Ashikha and Rose, Robert B.

and Grunden, Amy M. and Hofmann, Andreas}, abstractNote = {Bacterial α–carbonic anhydrases (α-CA) are zinc containing. Eriksson AE, Jones TA, Liljas A. Refined structure of human carbonic anhydrase II at A resolution. Proteins. ; 4 (4)– Fierke CA, Calderone TL, Krebs JF.

Functional consequences of engineering the hydrophobic pocket of carbonic anhydrase II. Biochemistry. Nov 19; 30 (46)–Cited by:   X-ray absorption studies of halide binding to carbonic anhydrase. Bengtsson U, Carlbom U, Fridborg K, Järup L, et al. Crystal structure of human erythrocyte carbonic anhydrase C.

The three-dimensional structure at high resolution in relation to other mammalian carbonic. The Carbon Dioxide Hydration Activity of these being one high specific activity form designated carbonic anhydrase C, and two, nearly identical low specific activity forms designated A and B.

high resolution crystal structures (7) give good promise for the. The prototype of the γ-class of carbonic anhydrase has been characterized from the methanogenic archaeon Methanosarcina thermophila.

Previously reported kinetic studies of the γ-class carbonic anhydrase are consistent with this enzyme having a reaction mechanism similar to that of the mammalian α-class carbonic anhydrase.

However, the overall folds of these two enzymes are. Abstract. The carbonic anhydrases are especially well suited for studies on molecular evolution for a variety of reasons: (1) In many mammals, two isozymes of carbonic anhydrase which appear to be products of two closely linked genes are present in the red by: [21 ] A.

Liljas, Crystal Structure Studies of Human Erythrocyte Carbonic Anhydrase C at High Resolution. Acta Universitatis Upsaliensis, Uppsala Dissertations from the Vol number 2 FEBS LETTERS August Faculty of Science 3 () (Almquist och Wiksell, Gamla Broga S 20 Stockholm, Sweden).

[22]Cited by:   The structure-thermodynamics correlation analysis was performed for a series of fluorine- and chlorine-substituted benzenesulfonamide inhibitors binding to several human carbonic anhydrase (CA) isoforms. The total of 24 crystal structures of 16 inhibitors bound to isoforms CA I, CA II, CA XII, and CA XIII provided the structural information of selective recognition between a Cited by: 4.

Human carbonic anhydrase II (HCA II) is a zinc-metalloenzyme that catalyzes the reversible interconversion of CO2 and HCO The rate-limiting step of this catalysis is the transfer of a proton between the Zn-bound solvent molecule and residue His In order to fully characterize the active site structural features implicated in the proton transfer mechanism, the refined X-ray crystal.

How to cite this article: Ghosh, C. et al. Targeting erythrocyte carbonic anhydrase and 18 O-isotope of breath CO 2 for sorting out type 1 and type Cited by: 4.

Purification and Properties of Human Erythrocyte Carbonic Anhydrases* (Received for publication, ) J. McD. volume of carbonic anhydrase B is found to be ml per it also gives superior resolution of the two major components, carbonic anhydrases B and C.

Oxygen NMR studies of carbonic anhydrase. Journal of the American Chemical Society(1), DOI: /jaa Y. Pocker and Simo Sarkanen.

Oxonase and esterase activities of erythrocyte carbonic anhydrase. Biochemistry17 (6), DOI: /bia A procedure for the large-scale preparation of human carbonic anhydrases B and C is described. The procedure has been adopted for routine use in this laboratory for preparing the large amounts of protein required for primary structural studies on both by:   Pocker, Y.

& Stone, J. The catalytic versatility of erythrocyte carbonic anhydrase. Kinetic studies of the enzyme-catalyzed hydrolysis of p-nitrophenyl acetate. Biochemistry. 6, – Author: Akram A. Da’dara, Andrea Angeli, Marta Ferraroni, Claudiu T. Supuran, Patrick J. Skelly.

Structure. The human CA1 protein contains an N-terminus active site, zinc binding site, pdf substrate-binding site. The pdf structure of the human CA1-bicarbonate anion complex reveals the geometry of two H-bonds between the GluThr pair and the GluHis pair, and one pi H-bond between a water molecule and the phenyl ring of the Tyr : BRENDA entry.High-resolution NMR spectroscopy has been used to study native carbonic anhydrase B unfolding with urea at pH and T = K.

The rigidity parameter reflecting the effectiveness of spin.Carbonic anhydrase II ebook name CA2), ebook one of sixteen forms of human α carbonic ic anhydrase catalyzes reversible hydration of carbon s in this enzyme are associated with osteopetrosis and renal tubular carbonic anhydrase allows the reabsorption of bicarbonate ions in the proximal tubule.

Loss of carbonic anhydrase activity in bones Aliases: CA2, CA-II, CAC, CAII, Car2, HEL, HEL-S .